text: Mitogen-activated protein kinase 1 (MAPK1) is also known as extracellular signal-regulated kinase 2 (ERK2). Two similar protein kinases with 85% sequence identity were originally called ERK1 and ERK2. They were found during a search for protein kinases that are rapidly phosphorylated after activation of cell surface tyrosine kinases such as the epidermal growth factor receptor. Phosphorylation of ERKs leads to the activation of their kinase activity.
  The molecular events linking cell surface receptors to activation of ERKs are complex. It was found that Ras GTP-binding proteins are involved in the activation of ERKs. Another protein kinase, Raf-1, was shown to phosphorylate a "MAP kinase-kinase", thus qualifying as a "MAP kinase kinase kinase". The MAP kinase-kinase, which activates ERK, was named "MAPK/ERK kinase" (MEK).
  Receptor-linked tyrosine kinases, Ras, Raf, MEK, and MAPK could be fitted into a signaling cascade linking an extracellular signal to MAPK activation. See: MAPK/ERK pathway.
  Transgenic gene knockout mice lacking MAPK1 have major defects in early development. Conditional deletion of Mapk1 in B cells showed a role for MAPK1 in T-cell-dependent antibody production. A dominant gain-of-function mutant of Mapk1 in transgenic mice showed a role for MAPK1 in T-cell development. Conditional inactivation of Mapk1 in neural progenitor cells of the developing cortex lead to a reduction of cortical thickness and reduced proliferation in neural progenitor cells.